Eugene A. Permyakov

5.0k total citations · 1 hit paper
138 papers, 4.0k citations indexed

About

Eugene A. Permyakov is a scholar working on Molecular Biology, Nutrition and Dietetics and Materials Chemistry. According to data from OpenAlex, Eugene A. Permyakov has authored 138 papers receiving a total of 4.0k indexed citations (citations by other indexed papers that have themselves been cited), including 98 papers in Molecular Biology, 31 papers in Nutrition and Dietetics and 20 papers in Materials Chemistry. Recurrent topics in Eugene A. Permyakov's work include Protein Structure and Dynamics (31 papers), Infant Nutrition and Health (22 papers) and Enzyme Structure and Function (19 papers). Eugene A. Permyakov is often cited by papers focused on Protein Structure and Dynamics (31 papers), Infant Nutrition and Health (22 papers) and Enzyme Structure and Function (19 papers). Eugene A. Permyakov collaborates with scholars based in Russia, United States and Finland. Eugene A. Permyakov's co-authors include Vladimir N. Uversky, Lawrence J. Berliner, Sergei E. Permyakov, Robert H. Kretsinger, Edward A. Burstein, Lina P. Kalinichenko, Anthony L. Fink, Alexander I. Denesyuk, Ekaterina L. Knyazeva and John Goers and has published in prestigious journals such as Journal of Biological Chemistry, SHILAP Revista de lepidopterología and PLoS ONE.

In The Last Decade

Eugene A. Permyakov

136 papers receiving 3.9k citations

Hit Papers

align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

Encyclopedia of Metalloproteins

2013 445 citations Vladimir N. Uversky, Eugene A. Permyakov et al. profile →

Peers

Eugene A. Permyakov

Phillip Greenspan United States

Masaaki Hirose Japan

Masahiro Takagi Japan

Antonio J. Pierik Germany

Feride Severcan Türkiye

Thomas J. Jess United Kingdom

Peter C. Maloney United States

Juha Rouvinen Finland

Aichun Dong United States

Phillip Greenspan United States

Eugene A. Permyakov

2.2k ×0.9

537 ×0.6

470 ×0.6

330 ×0.5

275 ×0.9

Citations per year, relative to Eugene A. Permyakov Eugene A. Permyakov (= 1×) peers Phillip Greenspan

Countries citing papers authored by Eugene A. Permyakov

Since Specialization

Citations

This map shows the geographic impact of Eugene A. Permyakov's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Eugene A. Permyakov with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Eugene A. Permyakov more than expected).

Fields of papers citing papers by Eugene A. Permyakov

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Eugene A. Permyakov. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Eugene A. Permyakov. The network helps show where Eugene A. Permyakov may publish in the future.

Co-authorship network of co-authors of Eugene A. Permyakov

This figure shows the co-authorship network connecting the top 25 collaborators of Eugene A. Permyakov. A scholar is included among the top collaborators of Eugene A. Permyakov based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Eugene A. Permyakov. Eugene A. Permyakov is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Denessiouk, Konstantin, Alexander I. Denesyuk, Sergei E. Permyakov, et al.. (2023). The active site of the SGNH hydrolase-like fold proteins: Nucleophile–oxyanion (Nuc-Oxy) and Acid–Base zones. SHILAP Revista de lepidopterología. 7. 100123–100123. 3 indexed citations

Permyakov, Sergei E., et al.. (2020). Mouse S100G protein exhibits properties characteristic of a calcium sensor. Cell Calcium. 87. 102185–102185. 4 indexed citations

Permyakov, Eugene A., et al.. (2016). Disorder in Milk Proteins: ? -Lactalbumin. Part A. Structural Properties and Conformational Behavior. Current Protein and Peptide Science. 17(4). 352–367. 13 indexed citations

Permyakov, Eugene A., Vladimir N. Uversky, & Sergei E. Permyakov. (2016). Interleukin-11: A Multifunctional Cytokine with Intrinsically Disordered Regions. Cell Biochemistry and Biophysics. 74(3). 285–296. 14 indexed citations

Uversky, Vladimir N., et al.. (2016). Disorder in Milk Proteins: ?-Lactalbumin. Part B. A Multifunctional Whey Protein Acting as an Oligomeric Molten Globular “Oil Container” in the Anti-Tumorigenic Drugs, Liprotides. Current Protein and Peptide Science. 17(6). 612–628. 11 indexed citations

Breydo, Leonid, Amanda Sales Conniff, Luísa A. Ferreira, et al.. (2015). Effects of osmolytes on protein-solvent interactions in crowded environment: Analyzing the effect of TMAO on proteins in crowded solutions. Archives of Biochemistry and Biophysics. 570. 66–74. 19 indexed citations

Kaspersen, Jørn Døvling, Jannik Nedergaard Pedersen, Søren B. Nielsen, et al.. (2014). Generic Structures of Cytotoxic Liprotides: Nano‐Sized Complexes with Oleic Acid Cores and Shells of Disordered Proteins. ChemBioChem. 15(18). 2693–2702. 35 indexed citations

Permyakov, Sergei E., et al.. (2014). Parvalbumin as a metal-dependent antioxidant. Cell Calcium. 55(5). 261–268. 6 indexed citations

Permyakov, Sergei E., et al.. (2011). Intrinsic disorder in S100 proteins. Molecular BioSystems. 7(7). 2164–2180. 29 indexed citations

10.

Permyakov, Sergei E., Evgeni Yu. Zernii, Ekaterina L. Knyazeva, et al.. (2011). Oxidation mimicking substitution of conservative cysteine in recoverin suppresses its membrane association. Amino Acids. 42(4). 1435–1442. 29 indexed citations

11.

Permyakov, Sergei E., et al.. (2010). Analysis of Ca²⁺/Mg²⁺ selectivity in α‐lactalbumin and Ca²⁺‐binding lysozyme reveals a distinct Mg²⁺‐specific site in lysozyme. Proteins Structure Function and Bioinformatics. 78(12). 2609–2624. 9 indexed citations

12.

Knyazeva, Ekaterina L., et al.. (2009). Interaction of antitumor α-lactalbumin—oleic acid complexes with artificial and natural membranes. Journal of Bioenergetics and Biomembranes. 41(3). 229–237. 33 indexed citations

13.

Permyakov, Sergei E., et al.. (2006). Calcium‐binding and temperature induced transitions in equine lysozyme: New insights from the pCa–temperature “phase diagrams”. Proteins Structure Function and Bioinformatics. 65(4). 984–998. 11 indexed citations

14.

Makhatadze, George I., Rikard Owenius, Vladimir N. Uversky, et al.. (2005). How to improve nature: study of the electrostatic properties of the surface of α-lactalbumin. Protein Engineering Design and Selection. 18(9). 425–433. 32 indexed citations

15.

Permyakov, Sergei E., Vladimir N. Uversky, Dmitry B. Veprintsev, et al.. (2001). Mutating aspartate in the calcium-binding site of α-lactalbumin: effects on the protein stability and cation binding. Protein Engineering Design and Selection. 14(10). 785–789. 23 indexed citations

16.

Veprintsev, Dmitry B., et al.. (1997). Cooperative thermal transitions of bovine and human apo‐α‐lactalbumins: evidence for a new intermediate state. FEBS Letters. 412(3). 625–628. 50 indexed citations

17.

Permyakov, Eugene A., et al.. (1993). Effects of Zn(II) on galactosyltransferase activity. Journal of Protein Chemistry. 12(5). 633–638. 12 indexed citations

18.

Permyakov, Eugene A., et al.. (1989). Interactions of parvalbumins with model phospholipid vesicles. Cell Calcium. 10(2). 71–79. 13 indexed citations

19.

Kalinichenko, Lina P., et al.. (1988). Environment of tryptophan residues in various conformational states of α-lactalbumin studied by time-resolved and steady-state fluorescence spectrosc. Biophysical Chemistry. 30(2). 105–112. 26 indexed citations

20.

Permyakov, Eugene A., et al.. (1971). Luminescence and the state of indole derivatives in frozen aqueous salt solutions. Journal of Structural Chemistry. 12(1). 65–71.

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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